2022
Pathogenic variants of sphingomyelin synthase SMS2 disrupt lipid landscapes in the secretory pathway
Sokoya T, Parolek J, Foged M, Danylchuk D, Bozan M, Sarkar B, Hilderink A, Philippi M, Botto L, Terhal P, Mäkitie O, Piehler J, Kim Y, Burd C, Klymchenko A, Maeda K, Holthuis J. Pathogenic variants of sphingomyelin synthase SMS2 disrupt lipid landscapes in the secretory pathway. ELife 2022, 11: e79278. PMID: 36102623, PMCID: PMC9531943, DOI: 10.7554/elife.79278.Peer-Reviewed Original ResearchConceptsSecretory pathwayER export signalPatient-derived fibroblastsFull enzymatic activityPhysical membrane propertiesExport signalSterol gradientLipid landscapeMammalian cellsCholesterol organizationLipid orderEnzymatic activityLipid distributionOsteogenic cellsPathwayBone phenotypeSMS2Glycerophospholipid profilePathogenic variantsCellsVariantsSphingomyelinSkeletal dysplasiaERSphingolipids
2019
Syndecan-1 Mediates Sorting of Soluble Lipoprotein Lipase with Sphingomyelin-Rich Membrane in the Golgi Apparatus
Sundberg EL, Deng Y, Burd CG. Syndecan-1 Mediates Sorting of Soluble Lipoprotein Lipase with Sphingomyelin-Rich Membrane in the Golgi Apparatus. Developmental Cell 2019, 51: 387-398.e4. PMID: 31543446, PMCID: PMC6832887, DOI: 10.1016/j.devcel.2019.08.014.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSphingomyelin-rich membranesTransmembrane domainSecretory pathwayVesicular transport carriersIntegral membrane proteinsProtein transmembrane domainBiosynthetic secretory pathwaySyndecan-1Heparan sulfate chainsLipoprotein lipaseSorting receptorSecretion pathwayMembrane proteinsGolgi membranesProteoglycan syndecan-1Protein cargoSecretory vesiclesPlasma membraneGolgi apparatusSpecific sequencesTransport carriersSulfate chainsLipid compositionEnzyme lipoprotein lipase